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Q4WL79

- BGLH_ASPFU

UniProt

Q4WL79 - BGLH_ASPFU

Protein

Probable beta-glucosidase H

Gene

bglH

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.By similarity

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei225 – 2251By similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00696.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable beta-glucosidase H (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase H
    Cellobiase H
    Gentiobiase H
    Gene namesi
    Name:bglH
    ORF Names:AFUA_6G14490
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 6

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 829829Probable beta-glucosidase HPRO_0000394879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi627 – 6271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi664 – 6641N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WL79.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini391 – 535145PA14Add
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family.Curated
    Contains 1 PA14 domain.Curated

    Phylogenomic databases

    eggNOGiCOG1472.
    HOGENOMiHOG000031215.
    KOiK01238.
    OMAiGCESTGV.
    OrthoDBiEOG7H799Q.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 2 hits.
    InterProiIPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    IPR011658. PA14.
    [Graphical view]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view]
    PRINTSiPR00133. GLHYDRLASE3.
    SMARTiSM00758. PA14. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q4WL79-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTPKFDIDYV LANITEDDKI ALLSGSDFWH THAIPKFNVP PIRTTDGPNG    50
    IRGTKFFAGV PAACLPCGTA LGATWDRDLL HQAGVLLGKE CLAKGAHCWL 100
    GPTINMQRSP LGGRGFESFA EDPHLSGIMA KSIILGCEST GVISTVKHYV 150
    GNDQEHERRA VDVLVTPRAL REIYLRPFQI VARDAHPGAL MTSYNKINGK 200
    HVVENPAMLD IVRKDWHWDP LIMSDWLGTY TTIDSLNAGL DLEMPGPTRY 250
    RGKYIESAMQ ARLIKQSTIS KRARKVLEFV ERASRAPVSA DETGRDFPED 300
    RALNRTLCAN SIVLLKNDGN LLPIPKTVKK IALIGSHVKT PAISGGGSAS 350
    LEPYYAVSLY DAVVEALPDA EILYEAGAYA HRMLPVIDRM LSNAVIHFYN 400
    EPPEKERTLL ATEPVVNTAF QLMDYNAPGL NRALFWATLI GEFTPDVSGL 450
    WDFGLTVFGT ATLFIDDEMV IDNATRQTRG TAFFGKGTVQ EVGQKQLTAG 500
    QTYKIRIEFG SANTSPMKAI GVVHFGGGAA HLGACLHMDP EQMVANAVRV 550
    AAEADYTIVC TGLNRDWESE GFDRPDMDLP PGIDALISSV LDVAADRTVI 600
    VNQSGTPVTM PWAHRARGIV QAWYGGNETG HGIADVLFGD VNPSGKLPLS 650
    WPADVRHNPT YLNNMSVGGR MLYGEDVYIG YRFYEKVGRE VLFPFGHGLS 700
    YTTFHVSPEA TVSPIVFSSD SPPTATVLVK NTGPMAGAQT LQLYIAAPNS 750
    ATPRPVKELH GFTKVFLQSG EERSVSIHID RYATSFWDEI EDMWKSEEGV 800
    YQVLIGTSSQ EIVSRGEFRV EQTRYWRGV 829
    Length:829
    Mass (Da):90,990
    Last modified:July 5, 2005 - v1
    Checksum:i9FC9D770D59A9ED9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000006 Genomic DNA. Translation: EAL89285.1.
    RefSeqiXP_751323.1. XM_746230.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00002146; CADAFUAP00002146; CADAFUAG00002146.
    GeneIDi3508640.
    KEGGiafm:AFUA_6G14490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000006 Genomic DNA. Translation: EAL89285.1 .
    RefSeqi XP_751323.1. XM_746230.1.

    3D structure databases

    ProteinModelPortali Q4WL79.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00002146 ; CADAFUAP00002146 ; CADAFUAG00002146 .
    GeneIDi 3508640.
    KEGGi afm:AFUA_6G14490.

    Phylogenomic databases

    eggNOGi COG1472.
    HOGENOMi HOG000031215.
    KOi K01238.
    OMAi GCESTGV.
    OrthoDBi EOG7H799Q.

    Enzyme and pathway databases

    UniPathwayi UPA00696 .

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    3.40.50.1700. 2 hits.
    InterProi IPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    IPR011658. PA14.
    [Graphical view ]
    PANTHERi PTHR30620. PTHR30620. 1 hit.
    Pfami PF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view ]
    PRINTSi PR00133. GLHYDRLASE3.
    SMARTi SM00758. PA14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiBGLH_ASPFU
    AccessioniPrimary (citable) accession number: Q4WL79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 55 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3